Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin-1

Gene

trxA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271Deprotonates C-terminal active site CysBy similarity
Active sitei33 – 331NucleophileBy similarity
Sitei34 – 341Contributes to redox potential valueBy similarity
Sitei35 – 351Contributes to redox potential valueBy similarity
Active sitei36 – 361NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciECOL386585:GJFA-4688-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-1
Short name:
Trx-1
Gene namesi
Name:trxA
Ordered Locus Names:Z5291, ECs4714
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 109108Thioredoxin-1PRO_0000120098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 36Redox-activePROSITE-ProRule annotation
Modified residuei70 – 701N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PRIDEiP0AA27.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi155864.Z5291.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Turni10 – 123Combined sources
Helixi13 – 175Combined sources
Beta strandi21 – 299Combined sources
Helixi34 – 4916Combined sources
Turni50 – 534Combined sources
Beta strandi54 – 607Combined sources
Turni61 – 633Combined sources
Helixi68 – 714Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 938Combined sources
Helixi97 – 10711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M7TNMR-A68-108[»]
1OAZX-ray2.78A/B2-109[»]
3DXBX-ray2.20A/B/C/D/E/F/G/H1-109[»]
5E4WX-ray2.80A/B3-109[»]
ProteinModelPortaliP0AA27.
SMRiP0AA27. Positions 2-109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA27.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 109108ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000292977.
KOiK03671.
OMAiMSEHIHY.
OrthoDBiEOG6QG8RK.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AA27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY
60 70 80 90 100
QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL

KEFLDANLA
Length:109
Mass (Da):11,807
Last modified:January 23, 2007 - v2
Checksum:iEF5933EA29668EE9
GO

Sequence cautioni

The sequence AAG58975.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB38137.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG58975.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB38137.1. Different initiation.
RefSeqiNP_312741.1. NC_002695.1.
WP_001280776.1. NZ_LPWC01000655.1.

Genome annotation databases

EnsemblBacteriaiAAG58975; AAG58975; Z5291.
BAB38137; BAB38137; BAB38137.
GeneIDi23335415.
915255.
KEGGiece:Z5291.
ecs:ECs4714.
PATRICi18359035. VBIEscCol44059_4676.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG58975.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB38137.1. Different initiation.
RefSeqiNP_312741.1. NC_002695.1.
WP_001280776.1. NZ_LPWC01000655.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M7TNMR-A68-108[»]
1OAZX-ray2.78A/B2-109[»]
3DXBX-ray2.20A/B/C/D/E/F/G/H1-109[»]
5E4WX-ray2.80A/B3-109[»]
ProteinModelPortaliP0AA27.
SMRiP0AA27. Positions 2-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z5291.

Proteomic databases

PRIDEiP0AA27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG58975; AAG58975; Z5291.
BAB38137; BAB38137; BAB38137.
GeneIDi23335415.
915255.
KEGGiece:Z5291.
ecs:ECs4714.
PATRICi18359035. VBIEscCol44059_4676.

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000292977.
KOiK03671.
OMAiMSEHIHY.
OrthoDBiEOG6QG8RK.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-4688-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AA27.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiTHIO_ECO57
AccessioniPrimary (citable) accession number: P0AA27
Secondary accession number(s): P00274
, P76750, Q47674, Q8XAT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.